Bound water structure and polymorphic amino acids act together to allow the binding of different peptides to MHC class I HLA-B53 (Q27732687)

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15 October 2019

title

Bound water structure and polymorphic amino acids act together to allow the binding of different peptides to MHC class I HLA-B53 (English)

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15 October 2019

5

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15 October 2019

Yvonne Jones

7

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15 October 2019

author name string

K J Smith

1

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15 October 2019

S W Reid

2

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15 October 2019

K Harlos

3

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15 October 2019

A J McMichael

4

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15 October 2019

J I Bell

6

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15 October 2019

publication date

1 March 1996

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15 October 2019

language of work or name

0 references

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15 October 2019

volume

4

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15 October 2019

issue

3

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15 October 2019

page(s)

215-228

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Sequence analysis of HLA-Bw53, a common West African allele, suggests an origin by gene conversion of HLA-B35

15 October 2019

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Recognition by CD8 on cytotoxic T lymphocytes is ablated by several substitutions in the class I alpha 3 domain: CD8 and the T-cell receptor recognize the same class I molecule

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Crystal structure of an H-2Kb-ovalbumin peptide complex reveals the interplay of primary and secondary anchor positions in the major histocompatibility complex binding groove

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Specificity pockets for the side chains of peptide antigens in HLA-Aw68

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Different length peptides bind to HLA-Aw68 similarly at their ends but bulge out in the middle

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Comparison of the P2 specificity pocket in three human histocompatibility antigens: HLA-A*6801, HLA-A*0201, and HLA-B*2705.

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Common west African HLA antigens are associated with protection from severe malaria

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Molecular analysis of the association of HLA-B53 and resistance to severe malaria

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7 January 2021

The antigenic identity of peptide-MHC complexes: A comparison of the conformations of five viral peptides presented by HLA-A2

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Substitution at residue 227 of H-2 class I molecules abrogates recognition by CD8-dependent, but not CD8-independent, cytotoxic T lymphocytes

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